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1NIR

OXYDIZED NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA

Summary for 1NIR
Entry DOI10.2210/pdb1nir/pdb
DescriptorNITRITE REDUCTASE, PHOSPHATE ION, CHLORIDE ION, ... (7 entities in total)
Functional Keywordsnitrite reductase, pseudomonas aeruginosa, hemoprotein, denitrification, domain swapping
Biological sourcePseudomonas aeruginosa
Cellular locationPeriplasm: P24474
Total number of polymer chains2
Total formula weight123474.94
Authors
Nurizzo, D.,Tegoni, M.,Cambillau, C. (deposition date: 1997-06-17, release date: 1997-12-03, Last modification date: 2024-10-16)
Primary citationNurizzo, D.,Silvestrini, M.C.,Mathieu, M.,Cutruzzola, F.,Bourgeois, D.,Fulop, V.,Hajdu, J.,Brunori, M.,Tegoni, M.,Cambillau, C.
N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa.
Structure, 5:1157-1171, 1997
Cited by
PubMed Abstract: Nitrite reductase from Pseudomonas aeruginosa (NiR-Pa) is a dimer consisting of two identical 60 kDa subunits, each of which contains one c and one d1 heme group. This enzyme, a soluble component of the electron-transfer chain that uses nitrate as a source of energy, can be induced by the addition of nitrate to the bacterial growth medium. NiR-Pa catalyzes the reduction of nitrite (NO2-) to nitric oxide (NO); in vitro, both cytochrome c551 and azurin are efficient electron donors in this reaction. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere.
PubMed: 9331415
DOI: 10.1016/S0969-2126(97)00267-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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